<big>'''This page is a simple compilation of all the news blurbs that have appeared on the ''CAZypedia'' [[Main Page]].'''</big>

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<big>This page is a simple compilation of all the news blurbs that have appeared on the ''CAZypedia'' [[Main Page]].</big>

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Revision as of 07:40, 10 February 2010

This page is a simple compilation of all the news blurbs that have appeared on the CAZypediaMain Page.

1 August 2019:Sweet Sixteen: The Carbohydrate Binding Module Family 16 page in CAZypedia has been flipped to Curator Approved today. The page features CBM16 members from two environmental bacteria with very different backgrounds: One bacterium was isolated from a red alga (red seaweed) and its GH16 kappa-carrageenase-appended CBM16 binds the red algal extracellular matrix polysaccharide carrageenan and influences the processive mechanism of the catalytic module. The other bacterium was isolated from organic waste leachate and deletion of both its CBM16s from a GH5 mannanase severely impairs binding ability of the catalytic module. The CBM16 page was Authored by Maria Matard-Mann with Elizabeth Ficko-Blean acting as Responsible Curator. Learn more about these "sweet sixteen" CBMs on the CBM16 page.

17 July 2019:A flashback on unsaturated glucuronyl hydrolases: Back in 2015, AuthorSeino Jongkees essentially completed the Glycoside Hydrolase Family 88 page, which was finally upgraded to Curator Approved status today. GH88 unsaturated glucuronyl hydrolases use an atypical glycoside hydrolase mechanism that involves the hydration of the double bond between carbons 4 and 5 of the non-reducing terminal sugar of their substrates and subsequent rearrangement. In this way, the activity of GH88 enzymes is dependent on the prior action of Polysaccharide Lyases to produce the required hexenuronic acid terminus. Learn more about these non-canonical enzymes, and their cousins in GH105, on the GH88 page.

14 May 2019:Starch... it's not over yet: Two new families of starch-binding CBMs, CBM82 and CBM83, have joined the CAZypedia ranks. These CBMs are both found in an enormous multi-modular cell-wall anchored enzyme from a gut bacterium. The pages were both authored by Darrell Cockburn with Nicole Koropatkin acting as responsible curator. Learn more about the new starch-binding CBM82 and CBM83 families on their respective pages.

28 February 2019:CE9 is CE page #2!: Graduate student Alex Anderson has completed CAZypedia's second Carbohydrate Esterase (CE) family page, Carbohydrate Esterase Family 9, which was Curator Approved by his supervisor Michael Suits today. CE9 enzymes are metal-dependent N-acetylglucosamine 6-phosphate deacetylases that function in peptidoglycan recycling in bacteria. CE9 is a huge family, currently comprising over 10,000 members (nearly all are from bacteria), which underscores their biological importance. Alex and Mike completed CAZypedia's first CE family page, CE4 earlier this month, and we thank them for these seminal expansions of of our resource. Learn more about the structure and mechanism of metal-dependent deamidases here: CE9, CE4.

27 November 2018:Remember, remember... an end of November new CAZypedia CBM family page. The type C L-rhamnose binding CBM67 family is now on-line in CAZypedia. Satoshi Kaneko authored the page and Harry Gilbert acted as responsible curator. Learn more about the structure and function of the CBM67 family on its CAZypedia page.

23 November 2018:Welcome to the CAZypedia fold CBM49! The crystalline cellulose-binding CBM49 CAZypedia page was authored by Breeanna Urbanowicz and Elizabeth Ficko-Blean. Breeanna Urbanowicz also acted as responsible curator. There is experimental evidence that rice CBM49 is cleaved post-translationally in vivo which probably plays an important role in plant growth. Find out more about the functionally interesting family 49 CBMs here.

11 October 2018:Fall ushers in a new CAZypedia CBM family page. The chitin-binding and lytic polysaccharide monooxygenase associated CBM73 family is described in detail. Zarah Forsberg authored the page and Gustav Vaaje-Kolstad acted as responsible curator. Learn more about the CBM73 family on its CAZypedia page.

24 September 2018:Revenge of the Ruminococci Part Deux. Two more CBM families from Ruminococcal bacteria are ready for reading. The CBM79 and CBM80 CAZypedia pages were authored by Immacolata Venditto and Harry Gilbert acted as responsible curator. These CBMs are important for enzyme targeting but also for targeting the entire cellulosome complex to substrate. More information on the CBM79 and CBM80 families can be found on their respective CAZypedia pages.

3 July 2018:Revenge of the Ruminococci. Three CBM families containing characterized CBM members from Ruminococcal bacteria are now on-line in CAZypedia; two of these families contain uniquely Ruminococcal CBMs. Ana Luis authored the pages (in one fell swoop) and Harry Gilbert acted as responsible curator. Descriptions of families CBM75, CBM76 and CBM77 can be found on their respective CAZypedia pages.

4 June 2018:When two worlds collide. The CBM81 family has an interesting binding mechanism, mixing characteristics of both type A and type B CBMs. The binding is enthalpically driven to soluble ligands, so by definition this is a type B interaction; however, the CBM binding face resembles the flat face of type A (crystalline-polysaccharide binding) CBMs. Marcelo Liberatoauthored the CBM81 page and Fabio Squina acted as the Responsible Curator. Find out more about the unusual family 81 CBMs here.

25 May 2018:The almost exclusive expansin associated CBM63 family is on-line. An interesting function is described as a bacterial CBM63 targets expansin to biomechanical hotspots in the Arabidopsis cell wall, where cell wall loosening occurs. The page was authored by Will Chase and Daniel Cosgrove with Daniel Cosgrove acting as responsible curator. Learn more about this expansin family CBM here.

4 May 2018:CAZypedia's first non-LPMO Auxiliary Activity Family page! Today Responsible CuratorRoland LudwigapprovedDaniel Kracher's and his expansive Auxiliary Activity Family 3 page. AA3 comprises a number of FAD-dependent redox enzymes including cellobiose dehydrogenase, aryl alcohol oxidase/dehydrogenases, glucose oxidases and glucose dehydrogenases, pyranose dehydrogenase, alcohol oxidase, and pyranose oxidase across four subfamilies. Roland and Daniel have done a monumental job in succinctly capturing the diversity of this family, which you can read about here.

2 May 2018:The CBM65 page has been added to the CAZypedia fold. This is a small CAZy family with two currently characterized members from an anaerobic cellulolytic ruminal bacterium. The two CBM65 members bind various beta-glucans and play an important role in enhancing enzymatic activity on substrate. The page was authored by Ana Luis and Harry Gilbert acted as responsible curator. Learn more about this CBM family here.

13 February 2018:The intricacies of pectin deconstruction: Rhamnogalacturonan II (RGII) represents the most structurally complex plant cell wall polysaccharide currently known, the complete saccharification of which requires a battery of CAZymes. Under the guidance of Responsible CuratorHarry Gilbert, four new GH pages related to RGII deconstruction were Curator Approved today. Special thanks go to AuthorsAna Luis (GH106, GH139, and GH141) and Didier Ndeh (GH138) for their hard work in putting these pages together. Learn more about the individual, specific contributions of each of these families (three of which have been recently uncovered) to microbial RGII utilization on their respective pages.

26 November 2017:CBM #1: Today, CBM pioneer Markus Linder completed the Carbohydrate Binding Module Family 1 page. CBM1 comprises the canonical fungal cellulose-binding modules (originally known as cellulose-binding domains), which were first found as stable cystine-knot-containing protein fragments released by controlled proteolysis of cellulases. The planar nature of the substrate-binding face, and linear arrangement of key aromatic residues, represent the archetype of CBMs that mediate glycosidase targeting to crystalline polysaccharides. Building on the original discovery of the modules now classified into CBM1 in Sweden, Markus Linder (then a Ph.D. student) and Tuula Teeri, working together across the Baltic Sea in Finland, were among the first to undertake structure-function studies and protein engineering of CBM1 using modern molecular techniques in the mid- to late-1990s. We're pleased to finally have this one in CAZYpedia - learn more about this seminal CBM family here.

11 October 2017:Ten years of CAZypedia! We are proud to announce the publication of a new article in Glycobiology in celebration of CAZypedia's tenth anniversary online. This article was written on behalf of all of present and future Contributors by Curators Harry Brumer and Spencer Williams, with input from a number of key individuals involved in the genesis of CAZypedia (see the Acknowledgements section for full details). A post-print version of the manuscript will be freely available from the UBC Library Open Collections, in addition to the final version on the Glycobiology website. Thanks to the hard work of a multitude of Contributors, CAZypedia is a successful example of community-driven, expert-based biocuration. We look forward to the continued development of this resource over the next ten years - and beyond!

10 September 2017:Sussing-out starch recognition in CBM58. We are excited to report that Nicole Koropatkin has completed the Carbohydrate Binding Module Family 58 page today. CBM58 constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as Bacteroides thetaiotaomicron. Within these bacteria, CBM58 modules are found inserted within the GH13 catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus). Nicole’s seminal structural biology has defined the family and provided insight into the recognition of amylose helices by CBM58 members in SusG homologs. Read more about this fascinating system here.

10 April 2017:A classic GH family. The Glycoside Hydrolase Family 22 page was completed today by Spencer Williams, with editorial input from Responsible CuratorDavid Vocadlo. GH22 contains the classic bacterial peptidoglycan hydrolase, hen egg-white lysozyme (HEWL), the first enzyme for which the three-dimensional structure was solved (reported in 1965). Moreover, seminal enzyme-carbohydrate complex structures have made HEWL a paradigm for glycosidases that operate through the classical Koshland retaining mechanism. Although the nature of the reaction intermediate remained contentious for many years since the original proposal of an oxacarbenium ion-carboxylate pair, a definitive study by Vocadlo, Davies, Laine, and Withers resolved the covalent nature of the glycosyl-enzyme HEWL in 2001, thus bringing mechanistic understanding of this classic enzyme in concordance with other retaining GH families. The lysozyme fold of HEWL defines the archetype for other hexosaminidases (i.e. those of GH19 and GH23) and the non-catalytic alpha-lactalbumins, and this fold notably has also been observed in recently emergent families of cellulases (GH124) and mannanases (GH134). Find out more about this classic GH family here!

3 November 2016:New PDB links-out. For 3-D visualization of exemplar CAZymes and CBMs, we're trying a switch from Proteopedia to the NGL viewer implementation at the RCSB Protein Data Bank. We've made this switch site-wide across CAZypedia, and would like to hear any feedback you might have. Here's an example for direct comparison: The seminal bacterial cellulose synthase complex in the JSMol viewer at Proteopedia (including wiki page) and in the NGL viewer at the PDB (other info available via the page tabs).

30 October 2016:Another X-module comes to light. Today Spencer Williams completed the Glycoside Hydrolase Family 135 page, which describes the genesis of a new CAZy family from a small group of modules formerly known as "X307" in the CAZyModO classification. The single biochemically and structurally characterized GH135 member hydrolyzes the unique fungal exo-polysaccharide galactosaminogalactan, with crystallographic evidence suggesting that the enzyme acts as a alpha-galactosaminidase. However, a number of key enzymological questions about this new family remain outstanding, and we look forward to future work in this direction of the CAZyme landscape.

3 September 2016:Galactosaminoglycan degradation.Spencer Williams has just completed a short entry on Glycoside Hydrolase Family 114, a small family of bacterial and fungal sequences currently represented by a single characterized endo-alpha-1,4-polygalactosaminidase. alpha-1,4-Polygalactosamine, also known as galactosaminoglycan, is produced as a secreted polysaccharide by select fungi, including Aspergilli.

27 February 2016:The sweet side of sulfur.AuthorSpencer Williams has updated the Glycoside Hydrolase Family 31 page to reflect the recent discovery of the first dedicated sulfoquinovosidases (SQases), previously ‘hidden’ within this family. SQases cleave α-glycosides of sulfoquinovose (6-sulfoglucose), which represent a significant reservoir of organosulfur in the biosphere. See the GH31 page to discover more of the hidden charms of this family.

6 August 2015:Live from the Cellulase/CAZyme GRC.CAZypedia marches on with the completion of the Polysaccharide Lyase Family 1 today by Responsible Curator and AuthorRichard Pickersgill, with additional editing by Polysaccharide Lyase Families coordinator Wade Abbott. PL1 contains pectate lyases from microbes and plants, which are key enzymes in plant cell wall remodelling/break-down. The solution of the crystal structure of a pectate lyase C from the plant pathogen Erwinia chrysanthemi was the first to reveal the parallel beta-helix as a novel protein fold that is now known to serve as the scaffold of other pectinolytic enzymes, including pectin hydrolases (GH28) and pectin methylesterases (CE8). Read more about the discovery of pectate lyases and the enzymology and crystallography of PL1here.

23 February 2015:The sites that bind.Birte Svensson and Darrell Cockburn have completed the Surface Binding Site page within the CAZypediaLexicon. Surface binding sites are substrate-binding regions found on the catalytic domain of carbohydrate-active enzymes and appear to play complementary roles to carbohydrate-binding modules in facilitating the action of polysaccharide-degrading glycoside hydrolases. Read more about these intriguing features and their distribution among CAZymes here.

20 February 2015:One for the Gals.Harry Gilbert has given the Carbohydrate Binding Module Family 62 page, which was authored by Cedric Montanier, Curator Approved status today. Functional and structural characterization of the archetypal CBM62 member from a Clostridium thermocellum xylanase revealed a strong affinity for galactose residues of either anomeric configuration on plant polysaccharides. Although the precise roles of this and other CBM62 members remains somewhat ambiguous, it is clear that these modules are relevant to the targeting of enzymes to the composite plant cell wall. Read more about the work of the all-star team that put CBM62 on the map (of CAZy families), here.

19 January 2015:Still in the high 70's today.Zui Fujimoto brought the Glycoside Hydrolase Family 78 page up to Curator Approved status today, making it CAZypedia's 97th approved GH page. GH78 is a family of archaeal, bacterial, and fungal alpha-L-rhamnosidases that cleave diverse flavonoid glycosides, polysaccharides, glycoproteins, and glycolipids from plants. Read more on these ecologically relevant enzymes here.

11 September 2014:Another PL family done. Today, Richard McLean and Wade Abbott finished the Polysaccharide Lyase Family 22 page, bringing the number of Curator ApprovedPL pages in CAZypedia to a total of 5 (of 23). PL22 is a family of bacterial (and a handful of archeal) oligogalacturonide lyases (OGLs), archetypal members of which are highly specific for digalacturonate and Δ4,5-unsaturated digalacturonate i.e., they do not cleave polymeric α-(1,4)-linked galacturonan, a component of pectin. Wade performed a seminal crystallographic analysis of PL22, and he and Richard have produced a lucid distillation of the mechanism of catalysis in this family. Read more here!

2 July 2014:More on the alpha-amylase clan. We are pleased to report that Stefan Janecek has made another key contribution to CAZypedia by completing the Glycoside Hydrolase Family 77 page today. GH77 contains enzymes variously known as amylomaltases, 4-α-glucanotransferases, or disproportionating enzymes (D-enzymes in plants), which catalyze (1-4)-to-(1-4) transglycosylation of alpha-glucan chains and form part of the starch/glycogen debranching system. Together with GH13 and GH70, GH77 constitutes Clan GH-H, a clan of alpha-glucan-specific enzymes united by a common (β/α)8 catalytic domain fold. Stefan is the founder and main organiser of ALAMY - the international symposia on the alpha-amylase enzyme family - and has been a key person in producing the GH13, GH70, GH77 pages in CAZypedia; we are especially grateful for all his hard work and expertise!

14 May 2014:Two new CBM pages. We are pleased to report that Shinya Fushinobu has produced and given Curator Approved status to two new CBM pages. Carbohydrate Binding Module Family 28 contains Type B CBMs that target non-crystalline beta-glucan chains, while Carbohydrate Binding Module Family 42 members are Type C CBMs that bind terminal, non-reducing-end L-arabinofuranosyl residues, as found in xylans. Both families are likely to play key role in potentiating biomass degradation by their host organisms, and are therefore relevant to related biotechnological applications.

6 February 2014:Our second LPMO page.Glyn Hemsworth and Gideon Davies have just completed the Auxiliary Activity Family 11 page. AA11 is a very recently discovered family of copper-dependent, lytic polysaccharide mono-oxygenases (LPMO), whose defining member catalyzes the oxidative cleavage of chitin. The LPMO field is particularly exciting and rapidly evolving, and we are proud to present the AA11 page in CAZypedia so closely after the initial report on this family.

18 December 2013:A new mannanase page. Today, Rohan Williams and Spencer Williams completed the Glycoside Hydrolase Family 113 page. GH113 is currently a very small family (120 members) with only one characterized member, the Alicyclobacillus acidocaldarius beta(1-4)-mannanase. The seminal crystal structure of this enzyme revealed GH113 to be a member of Clan GH-A. A recent publication from the Williams team and collaborators illuminated further details of the GH113 and GH26 transition states using designed inhibitor-enzyme complexes. Read more about this emerging family here!

6 October 2013:GH66 page upgraded to Curator Approved status. Today, Responsible CuratorZui Fujimoto formally approved the Glycoside Hydrolase Family 66 page, Authored by Ryuichiro Suzuki, as complete and ready for public viewing. GH66 is a very small family, currently containing ca. 60 members, of α(1-6)-glucan hydrolases (a.k.a. dextranases) and cyclo-isomalto-oligosaccharide glucanotransferases. Through a series of elegant studies including biochemical and crystallographic analyses, Dr. Fujimoto and his collaborators have provided direct insight into catalysis by this unique family. Read more about the long history of these enzymes here!

19 September 2013:We are proud to announce the completion of CAZypedia's first Auxiliary Activity (AA) Family page!Paul Harris, one of the founding fathers of the family previously known as GH61, has composed a lucid summary of the history and state-of-the-art of Auxiliary Activity Family 9. The revelation that these enzymes are actually copper-dependent lytic polysaccharide mono-oxygenases (LPMO), and not classic cellulases as originally thought, is one of the most exciting discoveries in enzymatic biomass degradation in recent years. Read more about this fascinating class of enzymes on the here, and stay tuned for forthcoming page on the closely related AA10 family.

28 June 2013:CAZypedia was highlighted in a review article in Current Opinion in Structural Biologyavailable online today. This review provides a succinct overview of some of the most exciting CAZyme structure-function studies in recent years, and we'd like to thank the authors, Shinya Fushinobu, Victor Alves, and Pedro Coutinho, for showcasing CAZypedia as well!

2 May 2013:Adding on to the Lexicon. Today Spencer Williams added the finishing touches to the Lexicon page on Transglycosylases. Transglycosylation - the ability to non-hydrolytically rearrange glycosidic bonds between one or more substrates - is a feature of many Glycoside hydrolases, especially those which use the retaining mechanism. In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation). Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant Transglycosylases. See the Lexicon page to learn more, including specific examples!

16 Jan 2013:Class I mannosidases × Williams2 = 90th CAZypedia GH page.Rohan Williams and Spencer Williams completed the Glycoside Hydrolase Family 47 page today to give CAZypedia its 90thCurator Approved GH page. GH47 is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes. Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD). Very few bacterial GH47 members are known, in contrast, and their function(s) has not been widely studied. From a mechanistic perspective, GH47 members are intriguing because the catalytic residues have not been unambiguously identified, despite high-resolution structure-function studies of these inverting enzymes. Check out the GH47 page to learn more!

14 Jan 2013:CAZypedia makes a contribution to MediaWiki community. We are proud to announce that BiblioPlus, an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the MediaWiki Extensions repository. BiblioPlus was coded by Karen Eddy, a UBC computer science student working with Harry Brumer, to resolve formatting issues with non-English characters in PubMed data. BiblioPlus is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. Thanks Karen, for all the hard work!

20 Nov 2012:A growing lexicon, II.Spencer Williams has upgraded the Glycosyltransferaseslexicon page to Curator Approved status today. This class of enzymes catalyzes the biosynthesis of the tremendous natural diversity of glycosides from activated sugar donor substrates and, as such, this page forms an essential part of CAZypedia'slexicon of terms and concepts. Thanks Spencer, for continuing to develop this resource!

16 Nov 2012:N-glycan deconstruction. There's been a flurry of activity on CAZypedia this past week; today, Al Boraston completed the Glycoside Hydrolase Family 125 page. GH125 was established last year based on a collaborative study between the Boraston and Vocadlo groups, which demonstrated that certain members from human bacterial pathogens can cleave alpha(1-6) mannosyl linkages typical of human N-glycans. Notably, GH125 members are also found in human gut symbiotic bacteria and pathogenic fungi, which underscores their potential biological importance in N-glycan deconstruction. Check out the GH125 page to read more about this new family, including a link to David and Al's seminal publication.

12 Nov 2012:Three new GH families. Thanks to our colleagues in Japan, three pages on recently established glycoside hydrolase families have been completed and given Curator Approved status in CAZypedia today. The GH121 and GH127 family pages by Kiyotaka Fujita describe Bifidobacterium longum enzymes involved in plant hydroxyproline-rich glycoprotein (HRGP) deconstruction. The GH129 page by Hisashi Ashida describes another family of Bifidobacterial enzymes, which in this case, appear to be involved in mucin glycoprotein degradation. Special thanks go to Responsible CuratorShinya Fushinobu for organizing the production of these important new pages!

05 Sep 2012:Transglucosylases. The Glycoside Hydrolase Family 70 page by Magali Remaud-Simeon has been copy-edited by Responsible CuratorStefan Janecek and given Curator Approved status today. GH70 comprises a family of enzymes with the notable ability to build high molecular weight α-glucan polysaccharides from sucrose as a glucosyl donor substrate. Depending the particular enzyme, α-1,2-; α-1,3-; α-1,4-; and/or α-1,6-linked glucans can be produced, which have applications in food, pharmaceutical, and fine chemical industries. In addition, biofilms of α-1,3-glucans produced by the GH70 enzymes of oral bacteria are also implicated in the formation of dental caries (cavities). Learn more about this interesting family of CAZymes here!

30 Apr 2012:A new cellulase fold. On April 27, Harry Gilbert completed the Glycoside Hydrolase Family 124 page here on CAZypedia.GH124 is a comparatively new, but tiny, family in the CAZy classification. This family is currently comprised of only three members (2 near-identical sequences from 2 Clostridium spp. and 1 from Ruminococcus albus), but was defined as a GH family based on the demonstration of cellulase activity in one of the Clostridial members. Remarkably, this enzyme was also shown to have a α8 superhelical fold, which has not been previously observed in cellulases, but is rather found in diverse lysozymes and lytic transglycosylases of GH23 active on bacterial cell wall peptidoglycan.

09 Mar 2012:β-glucuronidases!. Hot on the heels of their recent seminal structural and biochemical characterization of a Glycoside Hydrolase Family 79 β-glucuronidase, Hitomi Ichinose and Satoshi Kaneko have just completed the GH79 page in CAZypedia. GH79 is currently a rather small family comprised of enzymes from bacteria, fungi, plants, and mammals, which remove glucuronic acid (GlcA) or 4-O-methyl glucuronic acid from a diversity of substrates, ranging from secondary metabolites to structural biomolecules such as proteoglycans and arabinogalactan proteins. Click here to learn more about this interesting family!

11 Jan 2012:New for the new year.CAZypedia is proud to report that our first new page of 2012, the Glycoside Hydrolase Family 99 page, has been completed by Spencer Williams and given Curator Approved status today. This page follows the recent publication of seminal structural and mechanistic analyses by a multi-investigator team including CAZypedia Curators Spencer Williams and Gideon Davies, which suggests that endo-mannosidases of this family may use an unusual mechanism involving a 1,2-anhydro-β-mannopyranose ("sugar epoxide") intermediate to effect the release of Glc1–3-1,3-α-Man oligosaccharides during N-glycan trimming. GH99 is a small, but nonetheless important family, whose members come from both higher eukaryotes, which employ these enzymes in protein-folding quality-control, and bacteria, which are likely to use their homologues for carbohydrate scavenging in niche enviroments such as the human gut.

Also in the news:Spencer altered us to the fact that CAZypedia has clocked one million page views sometime recently. We're not quite sure what to make of that, but it seems like a pretty neat achievement. What is really interesting is that we are starting to see some dynamics in which pages are accessed most: Newer pages, such as GH18 (completed Oct. 2010), are becoming more popular than the very first CAZypedia page, GH1 (completed May 2007). And, some of the Lexicon pages, including those on the Cellulosome and anomeric configuration are right up there in the list. If you like to keep score, here's a list of our most popular pages. Want to find out when a particular CAZypedia page was Curator Approved? Click here.

18 July 2011:Our second GH-I chitosanase page.Ryszard Brzezinski has recently completed and Curator Approved his second page on chitosanases, enzymes which act specifically on the de-acetylated form of chitin (the polysaccharide chitin is a widespread in Nature as a main component of insect bodies and crustacean shells). Glycoside Hydrolase Family 80, a member of Clan GH-I together with GH24 and GH46, is a remarkably small family, which has thus far received only limited experimental attention. We therefore look forward to the expansion of this page with structural and mechanistic data in the future. Coincidentally, the GH80 page is our 80thCurator ApprovedGlycoside Hydrolase Family page in CAZypedia!

20 June 2011:More phosphorylases. On May 29, Author and Responsible CuratorHiroyuki Nakai completed the Glycoside Hydrolase Family 65 page. GH65 is comprised of alpha-glycoside phosphorylases and alpha,alpha-trehalose hydrolases. Due to the readily reversible nature of phosphorolysis, GH65 enzymes have been harnessed for glycoside synthesis, including recent work by Dr. Nakai. The completion of the GH65 complements previously completed pages on the beta-glycoside phosphorylases of GH94 and GH112 in CAZypedia.

12 May 2011:A new page on a new-ish family.Author and Responsible CuratorSatoshi Kaneko completed the Glycoside Hydrolase Family 115 page today. GH115 contains microbial alpha-glucuronidases, which are involved the cleavage of D-glucuronic acid and 4-O-methyl-D-glucuronic acid sidechains from xylans. Remarkably, GH115 enzymes can release these monosaccharides from intact polymer chains, which is rather rare for exo-acting enzymes, and contrasts them with glucuronidases from GH67. Although this regiospecific activity has been known since the last millenium, it was only in 2009 that these particular enzymes nucleated their own GH family.

09 May 2011:It's a big news day here at CAZypedia. We are proud to announce that three distinct glycoside hydrolase family pages have been Curator Approved today:

Glycoside Hydrolase Family 95 (written and curated by Takane Katayama) is a family of 1,2-α-L-fucosidases, members of which cleave human milk oligosaccharides, blood group glycoconjugates, and/or xyloglucan oligosaccharides.

Glycoside Hydrolase Family 117 (written by Etienne Rebuffet and curated by Mirjam Czjzek) is a small, newly created family of α-1,3-L-(3,6-anhydro)-galactosidases (neoagarobiose hydrolases), which catalyze the final step in the degradation of agars from red macroalgae in the marine environment.

We would like to express our sincere thanks to our Japanese and French colleagues for these important contributions to CAZypedia. Links to these families will be included in the next public update of the CAZy database (expected soon!).

Special thanks also go toEtiennefor updating theGlycoside Hydrolase Family 82page, including a very cool animated image that highlights enzyme domain movement during substrate binding - CAZypedia really is a living resource that can be continually improved with the latest knowledge.

28 April 2011:More on α-glucoside cleavage.Author and Responsible CuratorTakashi Tonozuka recently completed the Glycoside Hydrolase Family 63 page, which has been updated to Curator Approved status today. GH63 is especially notable as it contains the eukaryotic "processing α-glucosidase I enzymes," which are essential for N-glycan trimming during glycoprotein maturation. Takashi Tonozuka's group has done seminal structural elucidation work in this family, and we very much appreciate his contribution to CAZypedia, especially during these tough times in Japan.

21 March 2011:A new page on the equinox (as we thaw-out and welcome the sun back to the Baltic region).Responsible CuratorAnna Kulminskaya today approved the Glycoside Hydrolase Family 35 page, which was written by Anna, with input on the 3-D structure section from Mirko Maksimainen and Juha Rouvinen. GH35 is a family of β-galactosidases from diverse organisms that display a range of bond specificities. Only very few tertiary structures have been solved in this family, to which the Russian and Finnish groups have made seminal contributions.

28 February 2011:Hexosaminidases! The Glycoside Hydrolase Family 20 and Glycoside Hydrolase Family 84 pages, which were completed last week by AuthorIan Greig and approved by Responsible CuratorDavid Vocadlo, have today been cross-linked from the CAZy database(look out for the next public release). GH20 is of significant medical relevance, as it contains the human enzymes HexA and HexB, deficiencies of which case Tay-Sachs disease and Sandhoff diseases, respectively. GH84 is similarly important in the context of cell and organism biology, as this family contains human OGA (HexC, MGEA5, O-GlcNAcase), a nuclear and cytoplasmic enzyme that is responsible for dynamic modulation of β-linked O-GlcNAc residues linked to serine and threonine residues. O-GlcNAc'ylation of specific protein residues has in some cases been found to be reciprocal to phosphorylation and, accordingly, has implicated O-GlcNAc in diverse cellular processes and disease states.

07 February 2011:A landmark CAZypedia page. This one has been a long time coming, but today Birte Svensson and Stefan Janecek completed the Glycoside Hydrolase Family 13 page. GH13 is, quite simply, THE family of α-glucoside-degrading and -rearranging enzymes, with over 10000 members distributed into more than 35 subfamilies, which represent tens of enzyme activities. Due to the central role starch (amylose/amylopectin) and glycogen play in energy storage, these enzymes are of immense ecological and biotechnological importance. GH13 is also our 70th Curator Approved GH Family page!!!

17 January 2011:Our first news for the new year.Peter Reilly has just completed and approved the Glycoside Hydrolase Family 44 page. GH44 is another classic cellulase family (formerly known as cellulase family J); a number of these endo-beta(1-4)-glucanases have a penchant for degrading xyloglucan as well as soluble synthetic cellulose derivatives.

29 October 2010:News from sunny Provence.Florence Vincent has completed the Glycoside Hydrolase Family 73 page, which has just been edited and approved by Senior CuratorBernard Henrissat. GH73 contains peptidoglycan hydrolases with endo-β-N-acetylglucosaminidase (NAG, a.k.a. GlcNAc) specificity. Mechanistic and structural parallels between this family and other hexosaminidase families have been drawn, including GH18, whose CAZypedia page was very recently finished (see the preceding News item from Oct. 13).

13 October 2010:Gideon Davies has just completed and approved the Glycoside Hydrolase Family 18 chitinase/endo-β-N-acetylglucosaminidase page, with help from Nathalie Juge on the non-catalytic proteins in the family, which function as carbohydrate-binding proteins or enzyme inhibitors. Look out for links to this and several of the pages mentioned in previous News items in the latest version of the CAZy database, to be released today!

06 October 2010:Yet another classic cellulase family. The Glycoside Hydrolase Family 6 page by Kathleen Piens and Gideon Davies has just been upgraded to Curator Approved status. GH6 contains cellobiohydrolase II (CBHII, or Cel6A in the modern nomenclature), which is a main component of the enzyme cocktail secreted by the proficient cellulose-degrading organism, Hypocrea jecorica (née Trichoderma reesei).

11 August 2010:A new look. Today we upgraded the MediaWiki software that runs CAZypedia and switched the default interface to the shiny new Vector skin, which you may have already noticed on Wikipedia. Let us know if you find any problems with the new layout here. (If preferred, CAZypedians can actually still use the old default skin, Monobook, by logging in and changing their user preferences.)

8 July 2010:CAZypedia breaks new ground.CAZypedia has made its first foray into the world of glycosyltransferases with the GT42 page by Warren Wakarchuk. The Glycosyltransferase Families are still very much in a beta test stage, and we welcome input and ideas on the format of these pages.

We have finally fixed the problem with non-English characters in references from PubMed that was breaking some pages! We apologize for the delay and any inconvenience this may have caused.

18 May 2010:New from 日本: Curator Takashi Tonozuka has just completed and approved his page on the dextranase/pullulanase family GH49. Thanks go to Takashi for finishing the page despite our our ongoing troubles with PubMed references!

10 May 2010: Curator Yuval Shoham has just completed the Glycoside Hydrolase Family 51 page. GH51 is primarily an α-L-arabinofuranosidase family, whose members - like some GH43 enzymes - are involved in trimming the sidechains from plant xylans. These enzymes are therefore of potential interest in biomass processing.

16 April 2010:This just in via our news desk in Marseille.Vincent Eijsink has just finished and given Curator Approved status to our first chitinase page, Glycoside Hydrolase Family 19, following on the heels of the GH46chitosanase page completed in February. Vincent has included some very nice structure figures on the GH19 page, which add a nice splash of color and clarity.

7 March 2010: We are proud to announce that all four pages Curated by Anthony Clarke on peptidoglycan-degrading families have been Curator Approved and further improved over the past couple of weeks. So, in addition to GH23, which made the news on Feb. 18, CAZypedia now contains completed pages on GH102, GH103 and GH104!

22 January 2010:David Rose has just updated the references on the GH38 page with some recently published work on the role of cations in the active site, which gives us a good excuse to showcase this page (finished back in August 2009) here in the Latest News section. GH38 contains the Class II Golgi and lysosomal α-mannosidases involved in N-glycan processing on which David has done a lot of pioneering structural work. Thanks David!